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Nicotinamides, reduced

Diphosphopyridine nucleotide, reduced form Adenine-D-ribose-phosphate-phosphate D-ribose-nicotinamide, reduced form Cozymase, reduced form... [Pg.650]

High daily doses of pyridoxine can cause 35% reductions in phenytoin levels and 50% reductions in phenobarbital levels in some patients. Some evidence suggests that high doses of nicotinamide reduce the conversion of primidone to phenobarbital, and increase carbamazepine levels. [Pg.523]

Ammonia reacts with the ketone carbonyl group to give an mine (C=NH) which is then reduced to the amine function of the a ammo acid Both mine formation and reduc tion are enzyme catalyzed The reduced form of nicotinamide adenine diphosphonu cleotide (NADPH) is a coenzyme and acts as a reducing agent The step m which the mine is reduced is the one m which the chirality center is introduced and gives only L glutamic acid... [Pg.1124]

NADH is the reduced form of nicotinamide adenine dinucleotide. [Pg.526]

Insects poisoned with rotenone exhibit a steady decline ia oxygen consumption and the iasecticide has been shown to have a specific action ia interfering with the electron transport iavolved ia the oxidation of reduced nicotinamide adenine dinucleotide (NADH) to nicotinamide adenine dinucleotide (NAD) by cytochrome b. Poisoning, therefore, inhibits the mitochondrial oxidation of Krebs-cycle iatermediates which is catalysed by NAD. [Pg.270]

Glucose [50-99-7] urea [57-13-6] (qv), and cholesterol [57-88-5] (see Steroids) are the substrates most frequentiy measured, although there are many more substrates or metaboUtes that are determined in clinical laboratories using enzymes. Co-enzymes such as adenosine triphosphate [56-65-5] (ATP) and nicotinamide adenine dinucleotide [53-84-9] in its oxidized (NAD" ) or reduced (NADH) [58-68-4] form can be considered substrates. Enzymatic analysis is covered in detail elsewhere (9). [Pg.38]

Indicators There are certain compounds that are suitable as indicators for sensitive and specific clinical analysis. Nicotinamide adenine dinucleotide (NAD) occurs in oxidized (NAD" ) and reduced (NADH) forms. Nicotinamide adenine dinucleotide phosphate (NADP) also has two states, NADP" and NADPH. NADH has a very high uv—vis absorption at 339 nm, extinction coefficient = 6300 (M cm) , but NAD" does not. Similarly, NADPH absorbs light very strongly whereas NADP" does not. [Pg.38]

Fig. 9. Glucuionic acid pathway. NAD = nicotinamide-adenine dinucleotide NADH = reduced nicotinamide—adenine dinucleotide ... Fig. 9. Glucuionic acid pathway. NAD = nicotinamide-adenine dinucleotide NADH = reduced nicotinamide—adenine dinucleotide ...
NADP = nicotinamide-adenine dinucleotide phosphate NADPH = reduced nicotinamide—adenine dinucleotide phosphate NDP = nucleoside... [Pg.19]

Coenzymes such as adenosine diphosphate (ADP), adenosine SGtriphosphate (ATP), nicotinamide adenine dinucleotide (NAD), and nicotinamide adenine dinucleotide, reduced (NADH), are involved in some reactions (4). [Pg.392]

In oiological systems, the most frequent mechanism of oxidation is the remov of hydrogen, and conversely, the addition of hydrogen is the common method of reduc tion. Nicotinamide-adenine dinucleotide (NAD) and nicotinamide-adenine dinucleotide phosphate (NADP) are two coenzymes that assist in oxidation and reduction. These cofactors can shuttle between biochemical reac tions so that one drives another, or their oxidation can be coupled to the formation of ATP. However, stepwise release or consumption of energy requires driving forces and losses at each step such that overall efficiency suffers. [Pg.2133]

P-Nicotinamide adenine dinucleotide reduced di-Na salt trihydrate (reduced diphosphopyridine nucleotide sodium salt, NADH) [606-68-8] M 763.5, pK as for NAD. [Pg.551]

Nicotinamide adenine dinucleotide phosphate reduced tetrasodium salt (reduced diphosphopyridine nucleotide phosphate sodium salt, NADPH) [2646-71-1] M 833.4, pK as for NADP. Mostly similar to NADH above. [Pg.552]

Nicotinamide is an essential part of two important coenzymes nicotinamide adenine dinucleotide (NAD ) and nicotinamide adenine dinucleotide phosphate (NADP ) (Figure 18.19). The reduced forms of these coenzymes are NADH and NADPH. The nieotinamide eoenzymes (also known as pyridine nucleotides) are electron carriers. They play vital roles in a variety of enzyme-catalyzed oxidation-reduction reactions. (NAD is an electron acceptor in oxidative (catabolic) pathways and NADPH is an electron donor in reductive (biosynthetic) pathways.) These reactions involve direct transfer of hydride anion either to NAD(P) or from NAD(P)H. The enzymes that facilitate such... [Pg.588]

In living organisms, aldehyde and ketone reductions are carried out by either of the coenzymes NADH (reduced nicotinamide adenine dinucleotide) or NADPH (reduced nicotinamide adenine dinucleotide phosphate). Although... [Pg.610]

Reduced nicotinamide adenine dinucleotide, NADH, acts as the biological reducing agent. [Pg.932]

The first step in the biological degradation of lysine is reductive animation with a-ketoglutarate to give saccharopine. Nicotinamide adenine dinucleotide phosphate (NADPH), a relative of NADH, is the reducing agent. Show the mechanism. [Pg.1059]

Newman, Melvin S., 93 Newman projection, 93 molecular model of, 93 Nicotinamide adenine dinucleotide, biological oxidations with, 625-626 reactions of, 725 structure of, 725, 1044 Nicotinamide adenine dinucleotide (reduced), biological reductions with, 610-611... [Pg.1308]

All NOS isoforms utilize L-arginine as the substrate, and molecular oxygen and reduced nicotinamide adenine dinucleotide phosphate (NADPH) as cosubstrates. Flavin adenine dinucleotide (FMN), flavin mononucleotide (FAD), and (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4) are cofactors of the enzyme. All NOS isoforms contain heme and bind calmodulin. In nNOS and eNOS,... [Pg.862]


See other pages where Nicotinamides, reduced is mentioned: [Pg.169]    [Pg.187]    [Pg.767]    [Pg.131]    [Pg.169]    [Pg.187]    [Pg.767]    [Pg.131]    [Pg.274]    [Pg.645]    [Pg.646]    [Pg.1070]    [Pg.539]    [Pg.28]    [Pg.40]    [Pg.48]    [Pg.393]    [Pg.710]    [Pg.645]    [Pg.646]    [Pg.1070]    [Pg.591]    [Pg.125]    [Pg.365]    [Pg.270]    [Pg.809]    [Pg.724]    [Pg.1074]    [Pg.351]    [Pg.371]    [Pg.120]    [Pg.3]    [Pg.862]   
See also in sourсe #XX -- [ Pg.250 ]




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